Iontosorb CM
is a weakly acidic cation exchanger based on Bead
Cellulose with carboxylic functional groups:

The total volume capacity can be in the range 0.05 - 0.25
mmol/ml, the adequate mass capacity is 0.8 to 1.2 mmol/g dry matter. According to the customerīs demands the
sorbent volume capacity can be varied in the range given by the mass capacity and water
content. The water content of Iontosorb CM moves in the connection with the volume
capacity in the range 74 to 89 %.
Iontosorb CM is suitable for chromatographic separations of basic proteins, basic amino
acids, peptides, lipids and similar substances. Beside that, it may be used for enzyme
immobilization.
Applications of Iontosorb CM
Iontosorb CM can be used in the following applications:
ISOLATION AND CHARACTERISATION OF THE PROTEOLITIC ENZYMES OF CARP
HEPATOPANCREAS
M. Kminkova, Z. Moucka, Jiri Kucera
Potrav. vedy, 15 (1997) 351-362
 |
Trypsin and
Chymotripsyn activity in pooled fractions obtained from iontosorb CM
column (pH 6.0)
Column 2 x 8 cm equilibrated with 10 mM Tris-HCl pH
6.0 buffer, containing 10 mM calcium chloride
Adsorbed fractions were elued with 1 M NaCl in
starting buffer after washing-out the unadsorbed proteins. |
Original articles as full
texts are available in the information CD of the firm
Iontosorb.
USE OF BEAD CELLULOSE DERIVATIVES TO ISOLATION OF BACTERIAL ALKALINE
PROTEINASE BY COLUMN LIQUID CHROMATOGRAPHY
P. Gemeiner, V. Spanik, A. Snajdrova, E. Stratilova, M. Horvathova, D.
Hagarova and O. Markovic
Folia Microbiol. 36 (1991) 283-293
 |
Semi-preparative
ion exchange chromatography of alkaline proteinase on Iontosorb CM
The column 21 x 130 mm was equilibrated with phosphate buffer and
eluted with linear gradients of 0-0.5 and 0.5-1 mol/L NaCl,
respectively, in the above buffer; combined fractions (7-10) from
theproceding IEC dialyzed against phosphate buffer were loaded; the flow
rate 0.5 mL/min, 5 mL fractions were colected
N - fraction number, P - proteins (mg, circles), A620/h
- proteolytic activity (squares), NaCl gradient (mol/L, dashed
line). |
Original articles as full
texts are available in the information CD of the firm
Iontosorb.
MAGNETIC CATION EXCHANGE ISOLATION OF LYSOZYME FROM NATIVE HEG EGG WHITE
I. Safarik, Z. Sabatkova, O. Tokar, M. Safarikova
Food Technol. Biotechnol., 45 (2007) 355-359
 |
| Fast
protein liquid chromatography of original egg white (top), eluate from
Iontosorb MG CM 100 (middle) and eluate from Iontosorb MG SHP 100
(bottom) |
 |
Electrophoretic
patterns of egg white proteins and lysozyme isolated by Iontosorb MG CM
100
Lane 1- molecular mass markers; lane 2-egg white (9.3 ug of proteins
loaded); lane 3-egg white after finishing the adsorption process (8.1 ug
of proteins loaded); lane 4-lysozyme after elution from Iontosorb MG CM
100 (8.75 ug of proteins loaded); lane 5-commercial lysozyme (Fluka,
Germanny, 12 ug of proteins loaded). Arrow indicates the lysozyme
position. |
 |
Equilibrium
adsorption isotherms of hen egg white lysozyme using Iontosorb MG CM 100
(full triangles) and Iontosorb MG SHP 100 (full squares)
as adsorbents
Ceq - equilibrium liquid-phase concentration of the
unadsorbed (free) lysozyme; qeq - equilibrium solid-phase
concentration of the adsorbed lysozyme |
Original articles as full
texts are available in the information CD of the firm
Iontosorb or Isolation of LYSOZYME .
Technical Parameters
| Porozity Type |
Particle Size
[ um ] |
| CM 100 |
30 - 50 |
| 50 - 80 |
| 80 - 100 |
| 100 - 250 |
| 250 - 500 |
| CM 200 |
50 - 80 |
| 80 - 100 |
| 100 - 250 |
| 250 - 500 |
| CM 500 |
50 - 80 |
| 80 - 100 |
| 100 - 250 |
| 250 - 500 |
|